| Autor: |
Shi, Peng, Ren, Xiaoyu, Meng, Jie, Kang, Chenlu, Wu, Yihe, Rong, Yingxue, Zhao, Shujuan, Jiang, Zhaodi, Liang, Ling, He, Wanzhong, Yin, Yuxin, Li, Xiangdong, Liu, Yong, Huang, Xiaoshuai, Sun, Yujie, Li, Bo, Wu, Congying |
| Předmět: |
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| Zdroj: |
Nature Communications; 5/13/2022, Vol. 13 Issue 1, p1-14, 14p |
| Abstrakt: |
The folded mitochondria inner membrane-cristae is the structural foundation for oxidative phosphorylation (OXPHOS) and energy production. By mechanically simulating mitochondria morphogenesis, we speculate that efficient sculpting of the cristae is organelle non-autonomous. It has long been inferred that folding requires buckling in living systems. However, the tethering force for cristae formation and regulation has not been identified. Combining electron tomography, proteomics strategies, super resolution live cell imaging and mathematical modeling, we reveal that the mitochondria localized actin motor-myosin 19 (Myo19) is critical for maintaining cristae structure, by associating with the SAM-MICOS super complex. We discover that depletion of Myo19 or disruption of its motor activity leads to altered mitochondria membrane potential and decreased OXPHOS. We propose that Myo19 may act as a mechanical tether for effective ridging of the mitochondria cristae, thus sustaining the energy homeostasis essential for various cellular functions. The structure of the mitochondrial inner membrane, or cristae, is important for functional oxidative phosphorylation and energy production. Here, the authors show that loss of myosin 19 impairs cristae structure as well as energy production, connecting motor activity to membrane potential. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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